Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mechanism of misfolding of the human prion protein revealed by a pathological mutation.

Proceedings of the National Academy of Sciences of the United States of America - 23 Mar 2021

Sanz-Hernández Máximo, Barritt Joseph D, Sobek Jens, Hornemann Simone, Aguzzi Adriano, De Simone Alfonso

Abstract excerpt

The misfolding and aggregation of the human prion protein (PrP) is associated with transmissible spongiform encephalopathies (TSEs). Intermediate conformations forming during the conversion of the cellular form of PrP into its pathological scrapie conformation are key drivers of the misfolding process. Here, we analyzed the properties of the C-terminal domain of the human PrP (huPrP) and its T183A variant, which...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid
Share to Peptide Fragments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prion Diseases

Share to Prion Proteins

Share to Prions

Share to Protein Aggregation, Pathological

Share to Protein Folding

Share to Proteostasis Deficiencies

Source

Open in PubMed Open full text

Identifiers

PMID: 33731477
DOI: 10.1073/pnas.2019631118
PMCID: PMC7999870

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism of misfolding of the human prion protein revealed by a pathological mutation.PMID 33731477Read ↗

Influence of the pathogenic mutations T188K/R/A on the structural stability and misfolding of human prion protein: insight from molecular dynamics simulations.Semantic proximity Read ↗

Different misfolding mechanisms converge on common conformational changes: human prion protein pathogenic mutants Y218N and E196K.Semantic proximity Read ↗

Mutation-Dependent Refolding of Prion Protein Unveils Amyloidogenic-Related Structural Ramifications: Insights from Molecular Dynamics Simulations.Semantic proximity Read ↗

Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Semantic proximity Read ↗

The Pathogenic Mutation T182A Converts the Prion Protein into a Molten Globule-like Conformation Whose Misfolding to Oligomers but Not to Fibrils Is Drastically Accelerated.Semantic proximity Read ↗

Probing early misfolding events in prion protein mutants by NMR spectroscopy.Semantic proximity Read ↗

Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EMSemantic proximity Read ↗

Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.Semantic proximity Read ↗

Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.Semantic proximity Read ↗

Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation.Semantic proximity Read ↗

Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations.Semantic proximity Read ↗

Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich Dimer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.